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Cited by 1,929

The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.

The Galvanization of Biology: A Growing Appreciation for the Roles of Zinc

Berg, Jeremy M., Shi, Yigong·1996·Science

Abstract

Zinc ions are key structural components of a large number of proteins. The binding of zinc stabilizes the folded conformations of domains so that they may facilitate interactions between the proteins and other macromolecules such as DNA. The modular nature of some of these zinc-containing proteins has allowed the rational design of site-specific DNA binding proteins. The ability of zinc to be bound specifically within a range of tetrahedral sites appears to be responsible for the evolution of the wide range of zinc-stabilized structural domains now known to exist. The lack of redox activity for the zinc ion and its binding and exchange kinetics also may be important in the use of zinc for specific functional roles.

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Crossref · 10.1126/science.271.5252.1081

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Metadata

Authors
Berg, J. M., & Shi, Y.
Venue
Science
Published
1996-02-23
Volume
271
Issue
5252
Pages
1081-1085
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1992661805
Cited by
1,929
References
6
FWCI
23.01
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: The Galvanization of Biology: A Growing Appreciation for the Roles of Zinc. https://app.cochat.ai/papers/10.1126/science.271.5252.1081
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Berg, J. M., & Shi, Y. (1996). The Galvanization of Biology: A Growing Appreciation for the Roles of Zinc. Science. https://doi.org/10.1126/science.271.5252.1081

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.